AEP1_MESMA
ID AEP1_MESMA Reviewed; 85 AA.
AC P15228; Q9Y0B8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Toxin BmKAEP;
DE AltName: Full=Anti-epilepsy peptide;
DE AltName: Full=BmK AEP;
DE Flags: Precursor;
OS Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-75, AMIDATION AT GLY-82,
RP FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=11298767; DOI=10.1046/j.1432-1327.2001.02132.x;
RA Wang C.-G., He X.-L., Shao F., Liu W., Ling M.-H., Wang D.-C., Chi C.-W.;
RT "Molecular characterization of an anti-epilepsy peptide from the scorpion
RT Buthus martensi Karsch.";
RL Eur. J. Biochem. 268:2480-2485(2001).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 22-71, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=2930463; DOI=10.1042/bj2570509;
RA Zhou X.-H., Yang D., Zhang J.-H., Liu C.-M., Lei K.-J.;
RT "Purification and N-terminal partial sequence of anti-epilepsy peptide from
RT venom of the scorpion Buthus martensii Karsch.";
RL Biochem. J. 257:509-517(1989).
CC -!- FUNCTION: Shows anti-epileptic activity. Shares high homology with
CC depressant insect toxins, but shows very weak toxicity against mammals
CC and insects and no obvious symptoms on insect larvae. May target
CC voltage-gated sodium channel (Nav). {ECO:0000269|PubMed:11298767,
CC ECO:0000269|PubMed:2930463}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=6730.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11298767};
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR EMBL; AF160868; AAD43570.2; -; mRNA.
DR PIR; S02174; S02174.
DR AlphaFoldDB; P15228; -.
DR SMR; P15228; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; NAS:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR CDD; cd00107; Knot1; 1.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR018218; Scorpion_toxinL.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR PRINTS; PR00285; SCORPNTOXIN.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:11298767"
FT CHAIN 22..82
FT /note="Toxin BmKAEP"
FT /id="PRO_0000035212"
FT DOMAIN 22..82
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 82
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:11298767"
FT DISULFID 31..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 42..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 46..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT CONFLICT 29..30
FT /note="NG -> DN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="W -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63..64
FT /note="CW -> QD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="Q -> E (in Ref. 1; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="D -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 85 AA; 9296 MW; CC321DADAAEEF35E CRC64;
MKLFLLLVIS ASMLIDGLVN ADGYIRGSNG CKVSCLLGNE GCNKECRAYG ASYGYCWTWK
LACWCQGLPD DKTWKSESNT CGGKK
